Bitter tastant quinine modulates glucagon-like peptide-1 exocytosis from clonal GLUTag enteroendocrine L cells via actin reorganization

Harada, Kazuki; Sakaguchi, Hidekazu; Sada, Shoko; Ishida, Rika; Hayasaka, Yuki; Tsuboi, Takashi

doi:10.1016/j.bbrc.2018.04.143

Cited by 8 publications

(7 citation statements)

References 26 publications

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“… 35 Lysophosphatidyl inositol induces activation of the TRPV2 channel and increases intracellular calcium levels to trigger GLP-1 secretion. 36 The bitter tastant quinine modulates GLP-1 exocytosis via actin reorganization through elevation of intracellular calcium concentrations, 37 suggesting the involvement of ectopic bitter taste receptors in regulation of GLP-1 secretion in L cells.…”

Section: Discussionmentioning

confidence: 99%

Activation of ectopic olfactory receptor 544 induces GLP-1 secretion and regulates gut inflammation

Jeong

Kim

et al. 2021

Gut Microbes

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Section: Discussionmentioning

confidence: 99%

Activation of ectopic olfactory receptor 544 induces GLP-1 secretion and regulates gut inflammation

Jeong

Kim

et al. 2021

Gut Microbes

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“…enteroendocrine L cells, pancreatic β cells, neurons) may reflect the function of each cell in their physiological environments. Since we have previously found multiple effects of actin remodelling on GLP‐1 exocytosis [13,26], there should be a strict machinery promoting/restricting exocytosis through actin network, e.g. cortical F‐actin and stress fibres/focal adhesions.…”

Section: Discussionmentioning

confidence: 99%

“…GLP-1 secretion from L cells is achieved by exocytosis of GLP-1-containing granules. Intracellular second messenger molecules including Ca 2+ and cAMP, and cytoskeletons are major regulator of exocytosis [7][8][9], and recent studies have shown the importance of soluble NSF attachment protein receptor (SNARE) proteins and actin in the regulation of GLP-1 exocytosis [10][11][12][13]. During exocytosis of GLP-1, GLP-1containing granules in the cytoplasm are recruited and bound to the plasma membrane (docking).…”

mentioning

confidence: 99%

F‐actin determines the time‐dependent shift in docking dynamics of glucagon‐like peptide‐1 granules upon stimulation of secretion

et al. 2023

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Although exocytosis can be categorized into several forms based on docking dynamics, temporal regulatory mechanisms of the exocytotic forms are unclear. We explored the dynamics of glucagon-like peptide-1 (GLP-1) exocytosis in murine GLUTag cells (GLP-1-secreting enteroendocrine L-cells) upon stimulation with deoxycholic acid (DCA) or high K + to elucidate the mechanisms regulating the balance between the different types of exocytotic forms (pre-docked with the plasma membrane before stimulation; docked after stimulation and subsequently fused; or rapidly recruited and fused after stimulation, without stable docking). GLP-1 exocytosis showed a biphasic pattern, and we found that most exocytosis was from the pre-docked granules with the plasma membrane before stimulation, or granules rapidly fused to the plasma membrane without docking after stimulation. In contrast, granules docked with the plasma membrane after stimuli and eventually fused were predominant thereafter. Inhibition of actin polymerization suppressed exocytosis of the pre-docked granules. These results suggest that the docking dynamics of GLP-1 granules shows a time-dependent biphasic shift, which is determined by interaction with F-actin.

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“…This time-dependent shift of exocytotic dynamics was considered to be associated with cortical F-actin dynamics. Since we have previously found multiple effects of actin remodeling on GLP-1 exocytosis (Harada et al, 2018, 2017b), there should be a strict machinery promoting/restricting exocytosis through actin network, e.g. cortical F-actin and stress fibers/focal adhesions.…”

Section: Discussionmentioning

confidence: 99%

“…Studies on pancreatic β cells have revealed contribution of these molecules in spatial and temporal coordination of insulin exocytosis (Ma et al, 2020; Shibasaki et al, 2007; Yasuda et al, 2010; Yuan et al, 2015). Although there are several studies showing the importance of SNARE proteins and actin in the regulation of GLP-1 exocytosis (Campbell et al, 2020; Harada et al, 2018; Li et al, 2014; Wheeler et al, 2017), precise regulatory mechanism underlying exocytotic process of of GLP-1-containing granules is unknown.…”

Section: Introductionmentioning

confidence: 99%

Exocytotic dynamics of glucagon-like peptide-1 from enteroendocrine L cell line is regulated by actin polymerization

Harada

Takashima

Kitaguchi

et al. 2022

Preprint

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Stimulus-secretion coupling of glucagon-like peptide-1 (GLP-1) from enteroendocrine L cells is important for glucose homeostasis. Although intracellular second messengers including Ca2+ and cAMP, and cellular structures including actin cytoskeleton play roles in induction of exocytosis of GLP-1 granules, little is known about the specific part in the process of exocytosis in which they are involved. Here we explored the role of those molecules by live-cell imaging with mouse L cell line GLUTag cells, and used two stimuli: deoxycholic acid (DCA) and high K+. DCA increased both intracellular Ca2+ and cAMP levels, while high K+ only increased Ca2+. We next monitored a single exocytosis of GLP-1 granules and found that, during the first 10 minutes of stimulation, both stimuli mainly induced the exocytosis from the predocked granules with the plasma membrane before stimulation or granules immediately fused to the plasma membrane without docking. Furthermore, inhibition of actin polymerization suppressed the proportion of exocytosis by the predocked granules. These results suggest that the exocytotic process of GLP-1 granules is determined by interaction with F-actin upon the increase of either Ca2+ or cAMP.

show abstract

Bitter tastant quinine modulates glucagon-like peptide-1 exocytosis from clonal GLUTag enteroendocrine L cells via actin reorganization

Cited by 8 publications

References 26 publications

Activation of ectopic olfactory receptor 544 induces GLP-1 secretion and regulates gut inflammation

Activation of ectopic olfactory receptor 544 induces GLP-1 secretion and regulates gut inflammation

F‐actin determines the time‐dependent shift in docking dynamics of glucagon‐like peptide‐1 granules upon stimulation of secretion

Exocytotic dynamics of glucagon-like peptide-1 from enteroendocrine L cell line is regulated by actin polymerization

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